1988
DOI: 10.1111/j.1365-2621.1988.tb08943.x
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Preparation of Transparent Egg White Gel with Salt by Two‐step Heating Method

Abstract: A heat-induced transparent gel from egg white was prepared at low pH and low ionic strength by a one-step heating method. The addition of NaCl to the egg white formed a turbid gel on heating. Egg white, first diluted with water, gave a transparent solution upon heating of this mixture. The solution formed a transparent gel when heated with NaCl up to a concentration of 0.3M for a second time. The transparent gel obtained at 150 mM NaCl was more firm and less adhesive than the turbid gel prepared by the one-ste… Show more

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Cited by 27 publications
(11 citation statements)
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“…The formation of such aggregates is controlled by the balance between hydrophobic interaction and electrostatic repulsion for the denaturation and aggregation of protein by heat treatments (Kitabatake et al, 1987(Kitabatake et al, , 1988Matsudomi et al, 1991).…”
Section: Resultsmentioning
confidence: 99%
“…The formation of such aggregates is controlled by the balance between hydrophobic interaction and electrostatic repulsion for the denaturation and aggregation of protein by heat treatments (Kitabatake et al, 1987(Kitabatake et al, , 1988Matsudomi et al, 1991).…”
Section: Resultsmentioning
confidence: 99%
“…Our hypothesis is that the properties of egg albumin that have the potential to be oil‐retarding, i.e. its ability to form thermally induced gels , will be enhanced in the presence of corn and oat fiber because these fibers will act as plasticizers that affect thermogelation. The water holding properties of the fibers could interfere with the creation of pores in the deep fried food to reduce water migration that occurs with the absorption of oil.…”
Section: Introductionmentioning
confidence: 99%
“…PROTEIN GELS can be generally defined as 3-dimensional networks in which aggregate-aggregate and aggregate-solvent interactions occur in an ordered manner resulting in the immobilization of large amounts of water by a small proportion of protein (Phillips et al, 1994). Many investigators have been concerned with elucidating the mechanisms of heat-induced gelation of egg white proteins and the properties of such gels (Hatta et al, 1986;Hayakawa and Nakamura, 1986;Hegg, 1982;Kato et al, 1989Kato et al, , 1990aKitabatake et al, 1987Kitabatake et al, , 1988Mine, 1996;Tani et al, 1995). Globular proteins such as ovalbumin and lysozyme in simple systems, and egg white protein in a complex system have been considered to possess good gelling properties upon heating.…”
Section: Introductionmentioning
confidence: 99%
“…Manipulating factors such as pH, ionic strength, heating condition and protein concentration mainly produced two types of heat-induced protein gels, a transparent gel or a turbid gel. A two-step heating method was applied to the transparent gel formation (Kitabatake et al, 1987(Kitabatake et al, , 1988.…”
Section: Introductionmentioning
confidence: 99%